Enhancement of substrate recognition ability by combinatorial mutation of β-glucosidase displayed on the yeast cell surface

Applied Microbiology and Biotechnology

Volumn 76, Issue 5, 2007, Pages 1027-1033

  Fukuda, Takeshi ^a   Kato Murai, Michiko ^b   Kadonosono, Tetsuya ^b   Sahara, Hiroshi ^c   Hata, Yoji ^c   Suye, Shin Ichiro ^a   Ueda, Mitsuyoshi ^b  

^a UNIVERSITY OF FUKUI   (Japan)

^b KYOTO UNIVERSITY   (Japan)

^c Gekkeikan Sake Company Ltd   (Japan)

Author keywords

Comprehensive library of mutants; Family 3 glucosidase; SDW segment; Substrate recognition; Yeast cell surface engineering

Indexed keywords

AMINO ACIDS; CARBOXYLIC ACIDS; CATALYSIS; CELLS; GENETIC ENGINEERING; MUTAGENESIS; SUBSTRATES;

COMBINATORIAL MUTATION; HYDROLYTIC ACTIVITIES; HYDROLYTIC REACTION; YEAST CELL SURFACE ENGINEERING;

YEAST;

AROMATIC AMINO ACID; BETA GLUCOSIDASE;

AMINO ACID; CATALYSIS; ENZYME ACTIVITY; GENETIC ENGINEERING; MUTATION; SUBSTRATE PREFERENCE; YEAST;

AMINO ACID SEQUENCE; ARTICLE; ASPERGILLUS ORYZAE; BACTERIAL STRAIN; CATALYSIS; CELL LABELING; CELL SURFACE; CONTROLLED STUDY; ENZYME SUBSTRATE; FLUORESCENCE MICROSCOPY; FUNGAL STRAIN; FUNGUS MUTATION; GENETIC ENGINEERING; HYDROLYSIS; IMMUNOFLUORESCENCE; NONHUMAN; PLASMID; POLYMERASE CHAIN REACTION; YEAST CELL;

ASPERGILLUS ORYZAE; BETA-GLUCOSIDASE; BIOTECHNOLOGY; CATALYSIS; CELL MEMBRANE; GENE LIBRARY; GENETIC ENGINEERING; KINETICS; MUTATION; SACCHAROMYCES CEREVISIAE; SUBSTRATE SPECIFICITY;

ASPERGILLUS ORYZAE;

EID: 34548674030     PISSN: 01757598     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00253-007-1070-1     Document Type: Article

References (18)

1. Hanahan D (1983) Studies on transformation of Escherichia coli with plasmids. J Mol Biol 166:577-580
2. Henrissat B, Bairoch A (1993) New families in the classification of glycosyl hydrolases based on amino acid sequence similarities. Biochem J 293:781-788
3. Henrissat B, Bairoch A (1996) Updating the sequence-based classification of glycosyl hydrolases. Biochem J 316:695-696
4. Hrmova M, Fincher GB (2001) Structure-function relationships of β-d-glucan endo- and exohydrolases from higher plants. Plant Mol Biol 47:73-91
5. Hrmova M, MacGregor EA, Biely P, Stewart RJ, Fincher GB (1998) Substrate binding and catalytic mechanism of a barley β-d-glucosidase/(1,4)-β-d- glucan exohydrolase. J Biol Chem 273: 11134-11143
6. Iwashita K, Nagahara T, Kimura H, Takano M, Shimoi H, Ito K (1999) The bglA gene of Aspergillus kawachii encodes both extracellular and cell wall-bound β-glucosidases. Appl Environ Microbiol 65:5546-5553
7. Langston J, Sheehy N, Xu F (2006) Substrate specificity of Aspergillus oryzae family 3 β-glucosidase. Biochim Biophys Acta 1764:972-978
8. Li YK, Chir J, Chen FY (2001) Catalytic mechanism of a family 3 β-glucosidase and mutagenesis study on residue Asp-247. Biochem J 355:835-840
9. Li YK, Chir J, Tanaka S, Chen FY (2002) Identification of the general acid/base catalyst of a family 3 β-glucosidase from Flavobacterium meningosepticum. Biochemistry 41:2751-2759
10. Riou C, Salmon JM, Vallier MJ, Günata Z, Barre P (1998) Purification, characterization, and substrate specificity of a novel highly glucose-tolerant β-glucosidase from Aspergillus oryzae. Appl Environ Microbiol 64:3607-3614
11. Seidle HF, McKenzie K, Marten I, Shoseyov O, Huber RE (2005) Trp-262 is a key residue for the hydrolytic and transglucosidic reactivity of the Aspergillus niger family 3 β-glucosidase: substitution results in enzymes with mainly transglucosidic activity. Arch Biochem Biophys 444:66-75
12. Shibasaki S, Ueda M, Iizuka T, Hirayama M, Ikeda Y, Kamasawa N, Osumi M, Tanaka A (2001) Quantitative evaluation of the enhanced green fluorescent protein displayed on the cell surface of Saccharomyces cerevisiae by fluorometric and confocal laser scanning microscopic analyses. Appl Microbiol Biotechnol 55:471-475
13. Shiraga S, Kawakami M, Ueda M (2004) Construction of combinatorial library of starch-binding domain of Rhizopus oryzae glucoamylase and screening of clones with enhanced activity by yeast display method. J Mol Catal B Enzym 28:229-234
14. Tajima M, Nogi Y, Fukasawa T (1985) Primary structure of the Saccharomyces cerevisiae GAL7 gene. Yeast 1:67-77
15. Ueda M (2004) Future direction of molecular display by yeast-cell surface engineering. J Mol Catal B Enzym 28:139-143
16. Ueda M, Murai T, Shibasaki Y, Kamasawa N, Osumi M, Tanaka A (1998) Molecular breeding of polysaccharide-utilizing yeast cells by cell surface engineering. Ann NY Acad Sci 864:528-537
17. Vanderjagt DJ, Fry DE, Glew RH (1994) Human glucocerebrosidase catalyses transglucosylation between glucocerebroside and retinol. Biochem J 300:309-315
18. Varghese JN, Hrmova M, Fincher GB (1999) Three-dimensional structure of a barley β-d-glucan exohydrolase, a family 3 glycosyl hydrolase. Structure 7:179-190